luffa/arginine

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Isolation of lilin, a novel arginine- and glutamate-rich protein with potent antifungal and mitogenic activities from lily bulbs.

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From the dried bulbs of the lily (Lilium brownii), a protein with strong antifungal and mitogenic activities was isolated. It also exhibited an inhibitory action on the activity of HIV-1 reverse transcriptase. The protein was single-chained and possessed a molecular weight of 14.4 kDa and an

Isolation and molecular characterization of four arginine/glutamate rich polypeptides from the seeds of sponge gourd (Luffa cylindrica).

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Four arginine/glutamate rich polypeptides referred to as 5 k-, 6.5 k-, 12.5 k-, and 14 k-AGRPs were purified to homogeneity by gel filtration on Sephadex G-75 followed by CM-cellulose, butyl-Toyopearl 650 M, and reverse-phase HPLC from the seed of sponge gourd (Luffa cylindrica). Tricine SDS-PAGE

Primary structure of 6.5k-arginine/glutamate-rich polypeptide from the seeds of sponge gourd (Luffa cylindrica).

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The amino acid sequence of 6.5k-arginine/glutamate rich polypeptide (6.5k-AGRP) from the seeds of sponge gourd (Luffa cylindrica) has been determined. The 6.5k-AGRP consists of a 47-residue polypeptide chain containing two disulfide bonds, and a molecular mass calculated to be 5695 Da, which fully

Structural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica).

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Luffin P1, the smallest ribosome-inactivating peptide from the seeds of Luffa cylindrica was found to have anti-HIV-1 activity in HIV-1 infected C8166 T-cell lines and be able to bind with HIV Rev Response Element. Nuclear magnetic resonance spectroscopy revealed that the Luffin P1 comprises a

Trypsin inhibitors from ridged gourd (Luffa acutangula Linn.) seeds: purification, properties, and amino acid sequences.

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Two trypsin inhibitors, LA-1 and LA-2, have been isolated from ridged gourd (Luffa acutangula Linn.) seeds and purified to homogeneity by gel filtration followed by ion-exchange chromatography. The isoelectric point is at pH 4.55 for LA-1 and at pH 5.85 for LA-2. The Stokes radius of each inhibitor

Luffa acutangula agglutinin: Primary structure determination and identification of a tryptophan residue involved in its carbohydrate-binding activity using mass spectrometry.

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A lectin from phloem exudates of Luffa acutangula (ridge gourd) was purified on chitin affinity chromatography and characterized for its amino acid sequence and to study the role of tryptophan in its activity. The purified lectin was subjected to various proteolytic digestions, and the resulting

First Report of Pseudomonas cichorii Causing Leaf Spot of Vegetable Sponge Gourd in China.

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A suspect bacterial leaf spot on vegetable sponge gourd (Luffa cylindrical (L.) Roem.) was found in a commercial greenhouse in Pi County, Chengdu City, Sichuan Province, China, in February 2011. Approximately 20 to 30% of plants were affected, causing serious economic loss. Symptoms occurred only on

Isolation and partial characterization of three protein-synthesis inhibitory proteins from the seeds of Luffa cylindrica.

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Three new proteins which inhibit protein synthesis in rabbit reticulocyte lysates were isolated from an extract of sponge gourd (Luffa cylindrica) seeds by chromatography on a AF-Blue Toyopearl column followed by FPLC with a Mono S column. These three protein-synthesis inhibitory proteins (PSIs)

Luffangulin, a novel ribosome inactivating peptide from ridge gourd (Luffa acutangula) seeds.

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A ribosome inactivating peptide, with an N-terminal sequence exhibiting pronounced similarity to that of the 6.5 kDa-arginine/glutamate-rich polypeptide from Luffa cylindrica seeds, was isolated from seeds of a closely related species, the ridge gourd Luffa acutangula. The 5.6 kDa-peptide designated

Isolation and characterization of luffacylin, a ribosome inactivating peptide with anti-fungal activity from sponge gourd (Luffa cylindrica) seeds.

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A purification scheme involving ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, and ion exchange chromatography on CM-Sepharose and Mono S was employed to isolate a peptide with a molecular weight of 7.8kDa from sponge gourd seeds. The peptide, which was

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